CHST2 (carbohydrate sulfotransferase 2) is a Golgi-resident sulfotransferase that catalyzes the transfer of sulfate groups to position 6 of N-acetylglucosamine (GlcNAc) residues on N- and O-linked glycans 1. The enzyme uses 3'-phospho-5'-adenylyl sulfate (PAPS) as the sulfate donor and displays selective substrate specificity, preferentially sulfating terminal GlcNAc on the α1,3-mannose antenna of complex-type N-glycans and core 2 GlcNAc structures on O-linked mucin-type glycans 2. CHST2 works in concert with CHST1 and CHST4 to generate sialyl 6-sulfo Lewis X determinants (MECA-79 epitope) that serve as ligands for L-selectin on leukocytes, facilitating lymphocyte homing to peripheral lymph nodes 3. The enzyme is broadly expressed across tissues, with upregulation in vascular endothelial cells during inflammation 1. Beyond immune trafficking, CHST2-generated sulfated glycans function as recognition patterns for Siglecs and C-type lectins, modulating both immune surveillance and cell-cell interactions 4. CHST2 also contributes to sulfated ligand generation recognized by pathogenic bacteria; notably, Salmonella Typhi exploits CHST2-modified hepatobiliary glycans for tissue tropism 5. Elevated CHST2 expression correlates with poor prognosis in glioblastoma, identifying it as a potential therapeutic target 6.